Conformational Characterization of Intrinsically Disordered Proteins and Its Biological Significance
Open accessIntegrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Disordered proteins and regions are characterized by broad and heterogeneous ensembles with small differences in relative conformational stabilities and low barriers.
“Disordered proteins (regions) are characterized by broad and heterogeneous ensembles where the differences in the relative conformational stabilities are small, or even minor and the barriers are low.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [131]
Cites
Vicinal Proton Coupling in Nuclear Magnetic Resonance
Karplus, M. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00901a059 · Cited by 2,444 · see citing works
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001115)41:3 · Cited by 2,063 · see citing works
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1992) · Biochemistry · doi:10.1021/bi00121a010 · Cited by 2,057 · see citing works
Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010 · see citing works
Tjandra, N., & Bax, A. (1997) · Science · doi:10.1126/science.278.5340.1111 · Cited by 1,720 · see citing works
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,635 · see citing works
Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,406 · see citing works
Flexible nets: The roles of intrinsic disorder in protein interaction networks
Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122 · see citing works
Mechanism of coupled folding and binding of an intrinsically disordered protein
Sugase, K., Dyson, H. J., & Wright, P. E. (2007) · Nature · doi:10.1038/nature05858 · Cited by 1,040 · see citing works
Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012 · see citing works
Vuister, G. W., & Bax, A. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00070a024 · Cited by 990 · see citing works
Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
Nash, P., Tang, X., Orlicky, S. M., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T. J., & Tyers, M. (2001) · Nature · doi:10.1038/35107009 · Cited by 761 · see citing works
Introducing Protein Intrinsic Disorder
Habchi, J., Tompa, P., Longhi, S., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr400514h · Cited by 744 · see citing works
Marsh, J. A., Singh, V. K., Jia, Z., & Forman-Kay, J. D. (2006) · Protein Science · doi:10.1110/ps.062465306 · Cited by 730 · see citing works
Unfolded Proteins and Protein Folding Studied by NMR
Dyson, H. J., & Wright, P. E. (2004) · Chemical Reviews · doi:10.1021/cr030403s · Cited by 628 · see citing works
Sequence-Dependent Correction of Random Coil NMR Chemical Shifts
Schwarzinger, S., Kroon, G. J. A., Foss, T. R., Chung, J., Wright, P. E., & Dyson, H. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003760i · Cited by 604 · see citing works
RefDB: A database of uniformly referenced protein chemical shifts
Zhang, H., Neal, S., & Wishart, D. S. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1022836027055 · Cited by 448 · see citing works
Bernadó, P., Blanchard, L., Timmins, P. A., Marion, D., Ruigrok, R. W. H., & Blackledge, M. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506202102 · Cited by 436 · see citing works
Self-citationStructure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M. A., Tidow, H., Rutherford, T. J., Markwick, P. R. L., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M. J., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 420 · see citing works
Residual Dipolar Couplings in Structure Determination of Biomolecules
Prestegard, J. H., Bougault, C., & Kishore, A. I. (2004) · Chemical Reviews · doi:10.1021/cr030419i · Cited by 416 · see citing works
Smith, L. J., Bolin, K. A., Schwalbe, H., MacArthur, M. W., Thornton, J. M., & Dobson, C. M. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0041 · Cited by 385 · see citing works
Ozenne, V., Bauer, F., Salmon, L., Huang, J., Jensen, M. R., Segard, S., Bernadó, P., Charavay, C., & Blackledge, M. J. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts172 · Cited by 356 · see citing works
Self-citationDynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
Mittag, T., Orlicky, S. M., Choy, W., Tang, X., Lin, H., Sicheri, F., Kay, L. E., Tyers, M., & Forman-Kay, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809222105 · Cited by 338 · see citing works
Biophysical characterization of intrinsically disordered proteins
Eliezer, D. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.004 · Cited by 325 · see citing works
A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
Berliner, L. J., Grunwald, J., Hankovszky, H. O., & Hideg, K. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90612-1 · Cited by 316 · see citing works
Peng, J. W., & Wagner, G. (1992) · Biochemistry · doi:10.1021/bi00151a027 · Cited by 316 · see citing works
Sequence-Specific Random Coil Chemical Shifts of Intrinsically Disordered Proteins
Tamiola, K., Acar, B., & Mulder, F. A. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105656t · Cited by 315 · see citing works
NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins
Salmon, L., Nodet, G., Ozenne, V., Yin, G., Jensen, M. R., Zweckstetter, M., & Blackledge, M. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101645g · Cited by 304 · see citing works
Statistical coil model of the unfolded state: Resolving the reconciliation problem
Jha, A., Colubri, A., Freed, K. F., & Sosnick, T. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506078102 · Cited by 299 · see citing works
Jensen, M. R., Zweckstetter, M., Huang, J., & Blackledge, M. J. (2014) · Chemical Reviews · doi:10.1021/cr400688u · Cited by 298 · see citing works
Gillespie, J. R., & Shortle, D. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0954 · Cited by 297 · see citing works
Kjærgaard, M., & Poulsen, F. M. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9508-2 · Cited by 294 · see citing works
CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices
Baker, J. M., Hudson, R. P., Kanelis, V., Choy, W., Thibodeau, P. H., Thomas, P., & Forman-Kay, J. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1278 · Cited by 280 · see citing works
Constructing ensembles for intrinsically disordered proteins
Fisher, C. K., & Stultz, C. M. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.04.001 · Cited by 276 · see citing works
Henriques, J., Cragnell, C., & Skepö, M. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/ct501178z · Cited by 265 · see citing works
Arai, M., Sugase, K., Dyson, H. J., & Wright, P. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512799112 · Cited by 250 · see citing works
Defining Long-Range Order and Local Disorder in Native α-Synuclein Using Residual Dipolar Couplings
Bernadó, P., Bertoncini, C. W., Griesinger, C., Zweckstetter, M., & Blackledge, M. J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055538p · Cited by 241 · see citing works
Self-citationMukrasch, M. D., Markwick, P. R. L., Biernat, J., von Bergen�, M., Bernadó, P., Griesinger, C., Mandelkow�, E., Zweckstetter, M., & Blackledge, M. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0690159 · Cited by 222 · see citing works
Self-citationDescribing intrinsically disordered proteins at atomic resolution by NMR
Jensen, M. R., Ruigrok, R. W. H., & Blackledge, M. J. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.007 · Cited by 219 · see citing works
Intrinsically disordered proteins: emerging interaction specialists
Tompa, P., Schád, É., Tantos, Á., & Kalmár, L. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.08.009 · Cited by 215 · see citing works
Calculation of ensembles of structures representing the unfolded state of an SH3 domain
Choy, W., & Forman-Kay, J. D. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4750 · Cited by 213 · see citing works
pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins
Váradi, M., Kosol, S., Lebrun, P., Valentini, E., Blackledge, M. J., Dunker, A. K., Felli, I. C., Forman-Kay, J. D., Kriwacki, R. W., Pierattelli, R., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt960 · Cited by 211 · see citing works
Nodet, G., Salmon, L., Ozenne, V., Meier, S., Jensen, M. R., & Blackledge, M. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9069024 · Cited by 210 · see citing works
NMR studies of Brownian tumbling and internal motions in proteins
Korzhnev, D. M., Billeter, M., Arseniev, A. S., & Orekhov, V. (2001) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(00)00028-5 · Cited by 210 · see citing works
Structural Characterization of Intrinsically Disordered Proteins by NMR Spectroscopy
Kosol, S., Contreras-Martos, S., Cedeño, C., & Tompa, P. (2013) · Molecules · doi:10.3390/molecules180910802 · Cited by 199 · see citing works
Allison, J. R., Várnai, P., Dobson, C. M., & Vendruscolo, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904716h · Cited by 197 · see citing works
Cavalli, A., Camilloni, C., & Vendruscolo, M. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4793625 · Cited by 196 · see citing works
Protonless NMR Experiments for Sequence-Specific Assignment of Backbone Nuclei in Unfolded Proteins
Bermel, W., Bertini, I., Felli, I. C., Lee, Y., Luchinat, C., & Pierattelli, R. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0582206 · Cited by 193 · see citing works
Schwalbe, M., Ozenne, V., Bibow, S., Jaremko, M., Jaremko, Ł., Gajda, M. J., Jensen, M. R., Biernat, J., Becker, S., Mandelkow�, E., et al. (2013) · Structure · doi:10.1016/j.str.2013.10.020 · Cited by 192 · see citing works
Cell signaling, post-translational protein modifications and NMR spectroscopy
Theillet, F., Smet‐Nocca, C., Liokatis, S., Thongwichian, R., Kosten, J., Yoon, M., Kriwacki, R. W., Landrieu, I., Lippens, G. M., & Selenko, P. (2012) · Journal of Biomolecular NMR · doi:10.1007/s10858-012-9674-x · Cited by 188 · see citing works
Structural Reorganization of α-Synuclein at Low pH Observed by NMR and REMD Simulations
Wu, K., Weinstock, D. S., Narayanan, C., Levy, R. M., & Baum, J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.063 · Cited by 186 · see citing works
Mark, W.-Y., Liao, J. C. C., Lü, Y., Ayed, A., Laister, R. C., Szymczyna, B. R., Chakrabartty, A., & Arrowsmith, C. H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.045 · Cited by 175 · see citing works
Modeling Intrinsically Disordered Proteins with Bayesian Statistics
Fisher, C. K., Huang, A., & Stultz, C. M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105832g · Cited by 166 · see citing works
Characterization of disordered proteins with ENSEMBLE
Krzeminski, M., Marsh, J. A., Neale, C., Choy, W., & Forman-Kay, J. D. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts701 · Cited by 154 · see citing works
Jensen, M. R., Houben, K., Lescop, E., Blanchard, L., Ruigrok, R. W. H., & Blackledge, M. J. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801332d · Cited by 144 · see citing works
Schneider, R. C., Maurin, D., Communie, G., Kragelj, J., Hansen, D. F., Ruigrok, R. W. H., Jensen, M. R., & Blackledge, M. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja511066q · Cited by 143 · see citing works
Limits on Variations in Protein Backbone Dynamics from Precise Measurements of Scalar Couplings
Vögeli, B., Ying, J., Grishaev, A., & Bax, A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja070324o · Cited by 141 · see citing works
Automatic Assignment of the Intrinsically Disordered Protein Tau with 441-Residues
Narayanan, R. L., Dürr, U., Bibow, S., Biernat, J., Mandelkow�, E., & Zweckstetter, M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105657f · Cited by 135 · see citing works
Ramos, A., & Varani, G. (1998) · Journal of the American Chemical Society · doi:10.1021/ja982496e · Cited by 133 · see citing works
Determination of conformationally heterogeneous states of proteins
Vendruscolo, M. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.01.002 · Cited by 132 · see citing works
Interpreting Protein Structural Dynamics from NMR Chemical Shifts
Robustelli, P. J., Stafford, K. A., & Palmer, A. G. I. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300265w · Cited by 131 · see citing works
Mapping the Potential Energy Landscape of Intrinsically Disordered Proteins at Amino Acid Resolution
Ozenne, V., Schneider, R. C., Yao, M., Huang, J., Salmon, L., Zweckstetter, M., Jensen, M. R., & Blackledge, M. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306905s · Cited by 129 · see citing works
Explaining the Structural Plasticity of α-Synuclein
Ullman, O., Fisher, C. K., & Stultz, C. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja208657z · Cited by 126 · see citing works
Miskei, M., Antal, C., & Fuxreiter, M. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1019 · Cited by 119 · see citing works
NMR Analysis of a Tau Phosphorylation Pattern
Landrieu, I., Lacosse, L., Leroy, A., Wieruszeski, J., Trivelli, X., Sillen, A., Sibille, N., Schwalbe, H., Saxena, K., Langer, T., et al. (2006) · Journal of the American Chemical Society · doi:10.1021/ja054656+ · Cited by 117 · see citing works
Self-citationAbyzov, A., Salvi, N., Schneider, R., Maurin, D., Ruigrok, R. W. H., Jensen, M. R., & Blackledge, M. J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02424 · Cited by 117 · see citing works
On the Origin of Residual Dipolar Couplings from Denatured Proteins
Louhivuori, M., Pääkkönen, K., Fredriksson, K., Permi, P., Lounila, J., & Annila, A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja035427v · Cited by 113 · see citing works
Huang, J., & Grzesiek, S. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907974m · Cited by 112 · see citing works
Fitzkee, N. C., Fleming, P. J., & Rose, G. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20394 · Cited by 102 · see citing works
Plaxco, K. W., Morton, C. J., Grimshaw, S. B., Jones, J. A., Pitkeathly, M. C., Campbell, I. D., & Dobson, C. M. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018340217891 · Cited by 100 · see citing works
Biasio, A. D., de Opakua, A. I., Mortuza, G. B., Molina, R., Cordeiro, T. N., Castillo, F., Villate, M., Merino, N., Delgado, S., Gil‐Carton, D., et al. (2015) · Nature Communications · doi:10.1038/ncomms7439 · Cited by 98 · see citing works
Self-citationBibow, S., Ozenne, V., Biernat, J., Blackledge, M. J., Mandelkow�, E., & Zweckstetter, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205836j · Cited by 97 · see citing works
Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS
Sibille, N., & Bernadó, P. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120149 · Cited by 95 · see citing works
Self-citationAutomated Analysis of Protein NMR Assignments and Structures
Baran, M., Huang, Y. J., Moseley, H., & Montelione, G. T. (2004) · Chemical Reviews · doi:10.1021/cr030408p · Cited by 95 · see citing works
Partial alignment of biomolecules: an aid to NMR characterization
Prestegard, J. H., & Kishore, A. I. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00247-7 · Cited by 93 · see citing works
Sibille, N., Huvent, I., Fauquant, C., Verdegem, D., Amniai, L., Leroy, A., Wieruszeski, J., Lippens, G. M., & Landrieu, I. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23210 · Cited by 92 · see citing works
Self-citationYagi, H., Pilla, K. B., Maļeckis, A., Graham, B., Huber, T., & Otting, G. (2013) · Structure · doi:10.1016/j.str.2013.04.001 · Cited by 89 · see citing works
Small-angle scattering studies of intrinsically disordered proteins and their complexes
Cordeiro, T. N., Herranz-Trillo, F., Urbanek, A., Estaña, A., Cortés, J., Sibille, N., & Bernadó, P. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.011 · Cited by 84 · see citing works
Self-citationProtein flexibility, not disorder, is intrinsic to molecular recognition
Janin, J., & Sternberg, M. J. E. (2013) · F1000 Biology Reports · doi:10.3410/b5-2 · Cited by 79 · see citing works
Pérez, Y., Gairí, M., Pons, M., & Bernadó, P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.018 · Cited by 79 · see citing works
Self-citationSequence Context Influences the Structure and Aggregation Behavior of a PolyQ Tract
Eftekharzadeh, B., Piai, A., Chiesa, G., Mungianu, D., García, J., Pierattelli, R., Felli, I. C., & Salvatella, X. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.022 · Cited by 77 · see citing works
Mercadante, D., Milles, S., Fuertes, G., Svergun, D. I., Lemke, E. A., & Gräter, F. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b03440 · Cited by 77 · see citing works
Jorda, J., & Kajava, A. V. (2010) · Advances in protein chemistry and structural biology · doi:10.1016/s1876-1623(10)79002-7 · Cited by 75 · see citing works
Ganguly, D., & Chen, J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.019 · Cited by 72 · see citing works
Ordered Phosphorylation Events in Two Independent Cascades of the PTEN C-tail Revealed by NMR
Cordier, F., Chaffotte, A. F., Terrien, E., Prehaud, C. J. N., Theillet, F., Delepierre, M., Lafon, M., BUC, H. C., & Wolff, N. (2012) · Journal of the American Chemical Society · doi:10.1021/ja310214g · Cited by 66 · see citing works
Biasio, A. D., de Opakua, A. I., Cordeiro, T. N., Villate, M., Merino, N., Sibille, N., Lelli, M., Diercks, T., Bernadó, P., & Blanco, F. J. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.12.046 · Cited by 60 · see citing works
Self-citationRefinement of Ensembles Describing Unstructured Proteins Using NMR Residual Dipolar Couplings
Esteban-Martín, S., Fenwick, R. B., & Salvatella, X. (2010) · Journal of the American Chemical Society · doi:10.1021/ja906995x · Cited by 59 · see citing works
Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin α
Delaforge, E., Milles, S., Bouvignies, G., Bouvier, D., Boivin, S., Salvi, N., Maurin, D., Martel, A., Round, A. R., Lemke, E. A., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b07765 · Cited by 59 · see citing works
Self-citationHow a single residue in individual β‐thymosin/WH2 domains controls their functions in actin assembly
Didry, D., Cantrelle, F., Husson, C., Roblin, P., Moorthy, A. M. E., Pérez, J., Clainche, C. L., Hertzog, M., Guittet, É., Carlier, M., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.461 · Cited by 57 · see citing works
Mäntylahti, S., Hellman, M., & Permi, P. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9470-z · Cited by 54 · see citing works
NMR spin relaxation methods for characterization of disorder and folding in proteins
Bracken, C. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00136-4 · Cited by 52 · see citing works
Conformational averaging in structural biology: issues, challenges and computational solutions
Kruschel, D., & Žagrović, B. (2009) · Molecular BioSystems · doi:10.1039/b917186j · Cited by 42 · see citing works
Cordeiro, T. N., Chen, P., Biasio, A. D., Sibille, N., Blanco, F. J., Hub, J. S., Crehuet, R., & Bernadó, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1183 · Cited by 41 · see citing works
Self-citationOh, K., Lee, K., Park, E., Jung, Y., Hwang, G., & Cho, M. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24000 · Cited by 32 · see citing works
Fast hydrogen exchange affects 15N relaxation measurements in intrinsically disordered proteins
Kim, S., Wu, K., & Baum, J. (2013) · Journal of Biomolecular NMR · doi:10.1007/s10858-013-9706-1 · Cited by 23 · see citing works
Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins
Huang, J., Ozenne, V., Jensen, M. R., & Blackledge, M. J. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206585 · Cited by 22 · see citing works
Yao, X., Becker, S., & Zweckstetter, M. (2014) · Journal of Biomolecular NMR · doi:10.1007/s10858-014-9872-9 · Cited by 19 · see citing works
Okuda, M., & Nishimura, Y. (2015) · Oncogenesis · doi:10.1038/oncsis.2015.13 · Cited by 17 · see citing works
Seven Lessons from One IDP Structural Analysis
Uversky, V. N. (2010) · Structure · doi:10.1016/j.str.2010.08.003 · Cited by 15 · see citing works
Roche, J., Ying, J., & Bax, A. (2015) · Journal of Biomolecular NMR · doi:10.1007/s10858-015-0004-y · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
AlphaFold, Artificial Intelligence (AI), and Allostery
Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works
Baul, U., Bley, M., & Dzubiella, J. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c00546 · Cited by 29 · see citing works
The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection
Vieira, M. F. M., Hernandez, G., Zhong, Q., Arbesú, M., Veloso, T., Gomes, T., Martins, M. L., Monteiro, H., Frazão, C., Frankel, G., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05856-9 · Cited by 14 · see citing works
Self-citationToward a unified framework for determining conformational ensembles of disordered proteins
Ghafouri, H., Kadeřávek, P., Melo, A. M., Aspromonte, M. C., Bernadó, P., Cortés, J., Dosztányi, Z., Erdős, G., Feig, M., Janson, G., et al. (2026) · Nature Methods · doi:10.1038/s41592-026-03003-2 · Cited by 10 · see citing works
Self-citationIDPs and their complexes in GPCR and nuclear receptor signaling
Guillien, M., le Maire, A., Mouhand, A., Bernadó, P., Bourguet, W., Banères, J., & Sibille, N. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.05.001 · Cited by 9 · see citing works
Self-citationKim, M., Lee, J. H., & Jeong, K. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp03354c · Cited by 2 · see citing works
Vieira, M. F. M., Hernández, G., Veloso, T., Monteiro, H., Arbesú, M., Zanzoni, A., & Cordeiro, T. N. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.22.440577 · Cited by 1 · see citing works
Self-citation
- Authors
- Delaforge, E., Cordeiro, T. N., Bernadó, P., & Sibille, N.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Copenhagen (DK)
- Corresponding author
- Sibille, Nathalie
- Venue
- Modern Magnetic Resonance
- Publisher
- Springer International Publishing
- Published
- 2018
- Pages
- 381-399
- OpenAlex
- W4230174407
- Cited by
- 7
- References
- 100
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 1 · 2021: 1 · 2020: 2
- FWCI
- 1.01
- Type
- book chapter
- Language
- en
- Open access
- green
- hal.science
- Licence
- Locations
- Springer eBooks (publishedVersion)
- HAL (submittedVersion, other-oa)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- intrinsically disordered proteins, conformational plasticity, solvent accessibility, protein-protein recognition, signaling, cell regulation, post-translational modification, intramolecular interactions, NMR structural analysis, small-angle X-ray scattering, protein dynamics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review